data_5053
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of the Orphan PABC Domain from Saccharomyces cerevisiae
Poly(A)-binding Protein
;
_BMRB_accession_number 5053
_BMRB_flat_file_name bmr5053.str
_Entry_type original
_Submission_date 2001-06-12
_Accession_date 2001-06-12
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Kozlov Guennadi . .
2 Siddiqui Nadeem . .
3 Coillet-Matillon Stephane . .
4 Trempe Jean-Francois . .
5 Ekiel Irena . .
6 Sprules Tara . .
7 Gehring Kalle . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
coupling_constants 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 438
"13C chemical shifts" 174
"15N chemical shifts" 85
"coupling constants" 68
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2002-08-22 original author .
stop_
_Original_release_date 2002-08-22
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Solution Structure of the Orphan PABC Domain from Saccharomyces cerevisiae
Poly(A)-binding Protein
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22063288
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Kozlov Guennadi . .
2 Siddiqui Nadeem . .
3 Coillet-Matillon Stephane . .
4 Trempe Jean-Francois . .
5 Ekiel Irena . .
6 Sprules Tara . .
7 Gehring Kalle . .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_volume 277
_Journal_issue 25
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 22822
_Page_last 22828
_Year 2002
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_PABC_domain
_Saveframe_category molecular_system
_Mol_system_name 'C-terminal domain of Pab1p'
_Abbreviation_common 'PABC domain'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'PABC domain' $PABC
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_PABC
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'C-terminal domain of Pab1p'
_Abbreviation_common 'PABC domain'
_Molecular_mass 10434
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 92
_Mol_residue_sequence
;
GPLGSPRNANDNNQFYQQKQ
RQALGEQLYKKVSAKTSNEE
AAGKITGMILDLPPQEVFPL
LESDELFEQHYKEASAAYES
FKKEQEQQTEQA
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 2 PRO 3 LEU 4 GLY 5 SER
6 PRO 7 ARG 8 ASN 9 ALA 10 ASN
11 ASP 12 ASN 13 ASN 14 GLN 15 PHE
16 TYR 17 GLN 18 GLN 19 LYS 20 GLN
21 ARG 22 GLN 23 ALA 24 LEU 25 GLY
26 GLU 27 GLN 28 LEU 29 TYR 30 LYS
31 LYS 32 VAL 33 SER 34 ALA 35 LYS
36 THR 37 SER 38 ASN 39 GLU 40 GLU
41 ALA 42 ALA 43 GLY 44 LYS 45 ILE
46 THR 47 GLY 48 MET 49 ILE 50 LEU
51 ASP 52 LEU 53 PRO 54 PRO 55 GLN
56 GLU 57 VAL 58 PHE 59 PRO 60 LEU
61 LEU 62 GLU 63 SER 64 ASP 65 GLU
66 LEU 67 PHE 68 GLU 69 GLN 70 HIS
71 TYR 72 LYS 73 GLU 74 ALA 75 SER
76 ALA 77 ALA 78 TYR 79 GLU 80 SER
81 PHE 82 LYS 83 LYS 84 GLU 85 GLN
86 GLU 87 GLN 88 GLN 89 THR 90 GLU
91 GLN 92 ALA
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-28
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
PDB 1IFW "Solution Structure Of C-Terminal Domain Of Poly(A) Binding Protein From Saccharomyces Cerevisiae" 100.00 92 100.00 100.00 2.98e-58
DBJ BAA00017 "polyadenylate-binding protein [Saccharomyces cerevisiae]" 96.74 577 98.88 98.88 5.85e-50
DBJ GAA22994 "K7_Pab1p [Saccharomyces cerevisiae Kyokai no. 7]" 96.74 577 97.75 98.88 3.23e-49
EMBL CAY79353 "Pab1p [Saccharomyces cerevisiae EC1118]" 96.74 577 98.88 98.88 5.85e-50
GB AAA34787 "poly (A)-binding protein [Saccharomyces cerevisiae]" 96.74 577 98.88 98.88 5.85e-50
GB AAA34838 "polyadenylate-binding protein [Saccharomyces cerevisiae]" 96.74 577 98.88 98.88 5.97e-50
GB AAB64692 "Pab1p: polyadenylate-binding protein [Saccharomyces cerevisiae]" 96.74 577 98.88 98.88 5.85e-50
GB AAT92873 "YER165W [Saccharomyces cerevisiae]" 96.74 577 98.88 98.88 5.85e-50
GB AHY75721 "Pab1p [Saccharomyces cerevisiae YJM993]" 96.74 577 98.88 98.88 5.85e-50
REF NP_011092 "polyadenylate-binding protein [Saccharomyces cerevisiae S288c]" 96.74 577 98.88 98.88 5.85e-50
REF XP_011103263 "pab1p [Saccharomyces arboricola H-6]" 96.74 577 97.75 98.88 1.83e-49
SP P04147 "RecName: Full=Polyadenylate-binding protein, cytoplasmic and nuclear; Short=PABP; Short=Poly(A)-binding protein; AltName: Full=" 96.74 577 98.88 98.88 5.85e-50
TPG DAA07827 "TPA: polyadenylate-binding protein [Saccharomyces cerevisiae S288c]" 96.74 577 98.88 98.88 5.85e-50
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$PABC Yeast 4932 Eukaryota Fungi Saccharomyces cerevisiae
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$PABC 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$PABC 3.0 mM [U-15N]
NaCl 150 mM .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$PABC 3.0 mM .
NaCl 150 mM .
stop_
save_
save_sample_3
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$PABC 3.0 mM '[U-13C; U-15N]'
NaCl 150 mM .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name XWINNMR
_Version 2.1
loop_
_Task
'data collection'
stop_
_Details .
save_
save_GIFA
_Saveframe_category software
_Name GIFA
_Version 4.31
loop_
_Task
'data processing'
stop_
_Details .
save_
save_XEASY
_Saveframe_category software
_Name XEASY
_Version 1.3.13
loop_
_Task
'data analysis'
stop_
_Details .
save_
save_ARIA
_Saveframe_category software
_Name ARIA
_Version 0.9
loop_
_Task
'automated NOE assignment'
stop_
_Details .
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 0.9
loop_
_Task
refinement
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityPlus
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-1H_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_Sample_label .
save_
save_3D_1H-1H-15N_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-1H-15N NOESY'
_Sample_label .
save_
save_3D_1H-1H-15N_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-1H-15N TOCSY'
_Sample_label .
save_
save_3D_CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_Sample_label .
save_
save_3D_HNCACB_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-1H-15N NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-1H-15N TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.3 0.1 n/a
temperature 303 1 K
'ionic strength' 0.15 0.02 M
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
$sample_2
$sample_3
stop_
_Sample_conditions_label $conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PABC domain'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 2 PRO CA C 63.3 0.20 1
2 . 2 PRO HA H 4.47 0.02 1
3 . 2 PRO CB C 32.5 0.20 1
4 . 3 LEU N N 122.6 0.25 1
5 . 3 LEU H H 8.47 0.02 1
6 . 3 LEU CA C 55.6 0.20 1
7 . 3 LEU HA H 4.34 0.02 1
8 . 3 LEU CB C 42.5 0.20 1
9 . 3 LEU HB2 H 1.68 0.02 1
10 . 3 LEU HB3 H 1.68 0.02 1
11 . 4 GLY N N 110.1 0.25 1
12 . 4 GLY H H 8.35 0.02 1
13 . 4 GLY CA C 45.2 0.20 1
14 . 4 GLY HA2 H 3.96 0.02 1
15 . 4 GLY HA3 H 3.96 0.02 1
16 . 5 SER N N 117.2 0.25 1
17 . 5 SER H H 8.15 0.02 1
18 . 5 SER CA C 56.6 0.20 1
19 . 5 SER HA H 3.83 0.02 1
20 . 5 SER CB C 63.6 0.20 1
21 . 6 PRO CA C 63.5 0.20 1
22 . 6 PRO CB C 32.3 0.20 1
23 . 7 ARG N N 121.5 0.25 1
24 . 7 ARG H H 8.41 0.02 1
25 . 7 ARG CA C 56.5 0.20 1
26 . 7 ARG HA H 4.27 0.02 1
27 . 7 ARG CB C 30.9 0.20 1
28 . 7 ARG HB2 H 1.81 0.02 2
29 . 7 ARG HB3 H 1.73 0.02 2
30 . 7 ARG HG2 H 1.63 0.02 1
31 . 7 ARG HG3 H 1.63 0.02 1
32 . 8 ASN N N 120.2 0.25 1
33 . 8 ASN H H 8.43 0.02 1
34 . 8 ASN CA C 53.3 0.20 1
35 . 8 ASN HA H 4.69 0.02 1
36 . 8 ASN CB C 39.2 0.20 1
37 . 8 ASN HB2 H 2.86 0.02 2
38 . 8 ASN HB3 H 2.78 0.02 2
39 . 9 ALA N N 124.9 0.25 1
40 . 9 ALA H H 8.34 0.02 1
41 . 9 ALA CA C 53.3 0.20 1
42 . 9 ALA HA H 4.26 0.02 1
43 . 9 ALA CB C 19.4 0.20 1
44 . 9 ALA HB H 1.38 0.02 1
45 . 10 ASN N N 117.2 0.25 1
46 . 10 ASN H H 8.38 0.02 1
47 . 10 ASN CA C 53.6 0.20 1
48 . 10 ASN HA H 4.67 0.02 1
49 . 10 ASN CB C 38.9 0.20 1
50 . 10 ASN HB2 H 2.82 0.02 2
51 . 10 ASN HB3 H 2.72 0.02 2
52 . 11 ASP N N 120.6 0.25 1
53 . 11 ASP H H 8.09 0.02 1
54 . 11 ASP CA C 54.7 0.20 1
55 . 11 ASP HA H 4.57 0.02 1
56 . 11 ASP CB C 41.2 0.20 1
57 . 11 ASP HB2 H 2.67 0.02 1
58 . 11 ASP HB3 H 2.67 0.02 1
59 . 12 ASN N N 119.2 0.25 1
60 . 12 ASN H H 8.34 0.02 1
61 . 12 ASN CA C 53.8 0.20 1
62 . 12 ASN HA H 4.67 0.02 1
63 . 12 ASN CB C 38.9 0.20 1
64 . 12 ASN HB2 H 2.79 0.02 2
65 . 12 ASN HB3 H 2.68 0.02 2
66 . 13 ASN N N 119.2 0.25 1
67 . 13 ASN H H 8.36 0.02 1
68 . 13 ASN CA C 54.3 0.20 1
69 . 13 ASN HA H 4.66 0.02 1
70 . 13 ASN CB C 38.9 0.20 1
71 . 13 ASN HB2 H 2.84 0.02 1
72 . 13 ASN HB3 H 2.84 0.02 1
73 . 14 GLN N N 120.5 0.25 1
74 . 14 GLN H H 8.35 0.02 1
75 . 14 GLN CA C 57.4 0.20 1
76 . 14 GLN HA H 4.18 0.02 1
77 . 14 GLN CB C 28.9 0.20 1
78 . 14 GLN HB2 H 1.98 0.02 2
79 . 14 GLN HB3 H 1.94 0.02 2
80 . 14 GLN HG2 H 2.22 0.02 1
81 . 14 GLN HG3 H 2.22 0.02 1
82 . 15 PHE N N 120.3 0.25 1
83 . 15 PHE H H 8.14 0.02 1
84 . 15 PHE CA C 59.4 0.20 1
85 . 15 PHE HA H 4.47 0.02 1
86 . 15 PHE CB C 39.2 0.20 1
87 . 15 PHE HB2 H 3.05 0.02 1
88 . 15 PHE HB3 H 3.05 0.02 1
89 . 15 PHE HD1 H 7.12 0.02 3
90 . 16 TYR N N 120.2 0.25 1
91 . 16 TYR H H 8.01 0.02 1
92 . 16 TYR CA C 59.7 0.20 1
93 . 16 TYR HA H 4.36 0.02 1
94 . 16 TYR CB C 38.8 0.20 1
95 . 16 TYR HB2 H 3.06 0.02 2
96 . 16 TYR HB3 H 3.02 0.02 2
97 . 16 TYR HD1 H 7.12 0.02 3
98 . 16 TYR HE1 H 6.82 0.02 3
99 . 17 GLN N N 120.3 0.25 1
100 . 17 GLN H H 8.25 0.02 1
101 . 17 GLN CA C 57.6 0.20 1
102 . 17 GLN HA H 4.16 0.02 1
103 . 17 GLN HB2 H 2.17 0.02 2
104 . 17 GLN HB3 H 2.06 0.02 2
105 . 17 GLN HG2 H 2.42 0.02 1
106 . 17 GLN HG3 H 2.42 0.02 1
107 . 18 GLN N N 121.0 0.25 1
108 . 18 GLN H H 8.32 0.02 1
109 . 18 GLN CA C 58.5 0.20 1
110 . 18 GLN HA H 4.13 0.02 1
111 . 18 GLN CB C 28.7 0.20 1
112 . 18 GLN HB2 H 2.13 0.02 1
113 . 18 GLN HB3 H 2.13 0.02 1
114 . 18 GLN HG2 H 2.42 0.02 1
115 . 18 GLN HG3 H 2.42 0.02 1
116 . 19 LYS N N 120.7 0.25 1
117 . 19 LYS H H 8.23 0.02 1
118 . 19 LYS CA C 58.6 0.20 1
119 . 19 LYS HA H 4.11 0.02 1
120 . 19 LYS CB C 32.4 0.20 1
121 . 19 LYS HB2 H 1.80 0.02 1
122 . 19 LYS HB3 H 1.80 0.02 1
123 . 19 LYS HG2 H 1.43 0.02 2
124 . 19 LYS HG3 H 1.35 0.02 2
125 . 20 GLN N N 119.8 0.25 1
126 . 20 GLN H H 8.07 0.02 1
127 . 20 GLN CA C 58.2 0.20 1
128 . 20 GLN HA H 4.22 0.02 1
129 . 20 GLN CB C 29.4 0.20 1
130 . 20 GLN HB2 H 2.13 0.02 2
131 . 20 GLN HB3 H 2.04 0.02 2
132 . 20 GLN HG2 H 2.38 0.02 2
133 . 20 GLN HG3 H 2.29 0.02 2
134 . 21 ARG N N 121.0 0.25 1
135 . 21 ARG H H 8.17 0.02 1
136 . 21 ARG CA C 59.4 0.20 1
137 . 21 ARG HA H 4.03 0.02 1
138 . 21 ARG CB C 30.5 0.20 1
139 . 21 ARG HB2 H 1.88 0.02 1
140 . 21 ARG HB3 H 1.88 0.02 1
141 . 21 ARG HG2 H 1.70 0.02 2
142 . 21 ARG HG3 H 1.62 0.02 2
143 . 21 ARG HD2 H 3.21 0.02 1
144 . 21 ARG HD3 H 3.21 0.02 1
145 . 22 GLN N N 120.0 0.25 1
146 . 22 GLN H H 8.21 0.02 1
147 . 22 GLN CA C 58.6 0.20 1
148 . 22 GLN HA H 4.10 0.02 1
149 . 22 GLN CB C 28.6 0.20 1
150 . 22 GLN HB2 H 2.15 0.02 1
151 . 22 GLN HB3 H 2.15 0.02 1
152 . 22 GLN HG2 H 2.44 0.02 2
153 . 22 GLN HG3 H 2.40 0.02 2
154 . 23 ALA N N 123.1 0.25 1
155 . 23 ALA H H 7.96 0.02 1
156 . 23 ALA CA C 54.9 0.20 1
157 . 23 ALA HA H 4.25 0.02 1
158 . 23 ALA CB C 18.5 0.20 1
159 . 23 ALA HB H 1.52 0.02 1
160 . 24 LEU N N 120.2 0.25 1
161 . 24 LEU H H 8.16 0.02 1
162 . 24 LEU CA C 58.1 0.20 1
163 . 24 LEU HA H 4.08 0.02 1
164 . 24 LEU CB C 42.3 0.20 1
165 . 24 LEU HB2 H 1.74 0.02 2
166 . 24 LEU HB3 H 1.54 0.02 2
167 . 24 LEU HD1 H 0.69 0.02 2
168 . 24 LEU HD2 H 0.61 0.02 2
169 . 25 GLY N N 106.2 0.25 1
170 . 25 GLY H H 8.41 0.02 1
171 . 25 GLY CA C 48.5 0.20 1
172 . 25 GLY HA2 H 3.99 0.02 2
173 . 25 GLY HA3 H 3.65 0.02 2
174 . 26 GLU N N 122.1 0.25 1
175 . 26 GLU H H 8.02 0.02 1
176 . 26 GLU CA C 59.5 0.20 1
177 . 26 GLU HA H 4.12 0.02 1
178 . 26 GLU CB C 30.0 0.20 1
179 . 26 GLU HB2 H 2.19 0.02 2
180 . 26 GLU HB3 H 2.09 0.02 2
181 . 26 GLU HG2 H 2.45 0.02 1
182 . 26 GLU HG3 H 2.45 0.02 1
183 . 27 GLN N N 118.4 0.25 1
184 . 27 GLN H H 7.86 0.02 1
185 . 27 GLN CA C 58.8 0.20 1
186 . 27 GLN HA H 4.09 0.02 1
187 . 27 GLN CB C 29.4 0.20 1
188 . 27 GLN HB2 H 2.17 0.02 2
189 . 27 GLN HB3 H 2.12 0.02 2
190 . 27 GLN HG2 H 2.58 0.02 2
191 . 27 GLN HG3 H 2.42 0.02 2
192 . 28 LEU N N 120.8 0.25 1
193 . 28 LEU H H 8.72 0.02 1
194 . 28 LEU CA C 58.0 0.20 1
195 . 28 LEU HA H 3.93 0.02 1
196 . 28 LEU CB C 42.8 0.20 1
197 . 28 LEU HB2 H 1.76 0.02 2
198 . 28 LEU HB3 H 1.71 0.02 2
199 . 28 LEU HD1 H 0.92 0.02 1
200 . 28 LEU HD2 H 0.92 0.02 1
201 . 29 TYR N N 120.5 0.25 1
202 . 29 TYR H H 8.76 0.02 1
203 . 29 TYR CA C 61.6 0.20 1
204 . 29 TYR HA H 4.33 0.02 1
205 . 29 TYR CB C 38.7 0.20 1
206 . 29 TYR HB2 H 3.28 0.02 2
207 . 29 TYR HB3 H 3.03 0.02 2
208 . 29 TYR HD1 H 7.05 0.02 3
209 . 29 TYR HE1 H 6.64 0.02 3
210 . 30 LYS N N 119.2 0.25 1
211 . 30 LYS H H 7.64 0.02 1
212 . 30 LYS CA C 59.9 0.20 1
213 . 30 LYS HA H 3.83 0.02 1
214 . 30 LYS CB C 32.6 0.20 1
215 . 30 LYS HB2 H 1.92 0.02 1
216 . 30 LYS HB3 H 1.92 0.02 1
217 . 30 LYS HG2 H 1.71 0.02 1
218 . 30 LYS HG3 H 1.71 0.02 1
219 . 30 LYS HD2 H 1.49 0.02 1
220 . 30 LYS HD3 H 1.49 0.02 1
221 . 31 LYS N N 118.8 0.25 1
222 . 31 LYS H H 7.18 0.02 1
223 . 31 LYS CA C 59.4 0.20 1
224 . 31 LYS HA H 3.84 0.02 1
225 . 31 LYS CB C 32.8 0.20 1
226 . 31 LYS HB2 H 1.43 0.02 2
227 . 31 LYS HB3 H 0.97 0.02 2
228 . 31 LYS HG2 H 1.34 0.02 1
229 . 31 LYS HG3 H 1.34 0.02 1
230 . 32 VAL N N 120.2 0.25 1
231 . 32 VAL H H 8.54 0.02 1
232 . 32 VAL CA C 67.1 0.20 1
233 . 32 VAL HA H 3.56 0.02 1
234 . 32 VAL CB C 32.3 0.20 1
235 . 32 VAL HB H 2.07 0.02 1
236 . 32 VAL HG1 H 1.25 0.02 2
237 . 32 VAL HG2 H 1.09 0.02 2
238 . 33 SER N N 115.4 0.25 1
239 . 33 SER H H 8.76 0.02 1
240 . 33 SER CA C 61.0 0.20 1
241 . 33 SER HA H 4.17 0.02 1
242 . 33 SER CB C 62.7 0.20 1
243 . 33 SER HB2 H 3.68 0.02 2
244 . 33 SER HB3 H 3.30 0.02 2
245 . 34 ALA N N 121.1 0.25 1
246 . 34 ALA H H 6.88 0.02 1
247 . 34 ALA CA C 53.7 0.20 1
248 . 34 ALA HA H 4.20 0.02 1
249 . 34 ALA CB C 18.7 0.20 1
250 . 34 ALA HB H 1.41 0.02 1
251 . 35 LYS N N 115.9 0.25 1
252 . 35 LYS H H 7.52 0.02 1
253 . 35 LYS CA C 56.0 0.20 1
254 . 35 LYS HA H 4.24 0.02 1
255 . 35 LYS CB C 34.0 0.20 1
256 . 35 LYS HB2 H 1.72 0.02 1
257 . 35 LYS HB3 H 1.72 0.02 1
258 . 35 LYS HG2 H 1.32 0.02 1
259 . 35 LYS HG3 H 1.32 0.02 1
260 . 35 LYS HD2 H 1.55 0.02 1
261 . 35 LYS HD3 H 1.55 0.02 1
262 . 36 THR CA C 60.4 0.20 1
263 . 36 THR HA H 4.63 0.02 1
264 . 36 THR CB C 70.3 0.20 1
265 . 36 THR HG2 H 1.18 0.02 1
266 . 37 SER H H 8.46 0.02 1
267 . 37 SER CA C 58.7 0.20 1
268 . 37 SER HA H 4.49 0.02 1
269 . 37 SER CB C 63.7 0.20 1
270 . 37 SER HB2 H 4.04 0.02 2
271 . 37 SER HB3 H 3.93 0.02 2
272 . 38 ASN N N 120.6 0.25 1
273 . 38 ASN H H 7.90 0.02 1
274 . 38 ASN CA C 53.3 0.20 1
275 . 38 ASN HA H 4.22 0.02 1
276 . 38 ASN CB C 39.7 0.20 1
277 . 38 ASN HB2 H 2.95 0.02 2
278 . 38 ASN HB3 H 2.86 0.02 2
279 . 38 ASN ND2 N 114.1 0.25 1
280 . 38 ASN HD21 H 7.79 0.02 2
281 . 38 ASN HD22 H 7.17 0.02 2
282 . 39 GLU N N 127.4 0.25 1
283 . 39 GLU H H 9.01 0.02 1
284 . 39 GLU CA C 60.0 0.20 1
285 . 39 GLU HA H 4.08 0.02 1
286 . 39 GLU CB C 30.0 0.20 1
287 . 39 GLU HB2 H 2.12 0.02 1
288 . 39 GLU HB3 H 2.12 0.02 1
289 . 39 GLU HG2 H 2.44 0.02 1
290 . 39 GLU HG3 H 2.44 0.02 1
291 . 40 GLU N N 123.1 0.25 1
292 . 40 GLU H H 8.33 0.02 1
293 . 40 GLU CA C 59.7 0.20 1
294 . 40 GLU HA H 4.13 0.02 1
295 . 40 GLU CB C 29.4 0.20 1
296 . 40 GLU HB2 H 2.23 0.02 1
297 . 40 GLU HB3 H 2.23 0.02 1
298 . 40 GLU HG2 H 2.35 0.02 1
299 . 40 GLU HG3 H 2.35 0.02 1
300 . 41 ALA N N 123.1 0.25 1
301 . 41 ALA H H 7.99 0.02 1
302 . 41 ALA CA C 54.7 0.20 1
303 . 41 ALA HA H 3.35 0.02 1
304 . 41 ALA CB C 18.6 0.20 1
305 . 41 ALA HB H 1.26 0.02 1
306 . 42 ALA N N 118.8 0.25 1
307 . 42 ALA H H 8.45 0.02 1
308 . 42 ALA CA C 55.3 0.20 1
309 . 42 ALA HA H 3.81 0.02 1
310 . 42 ALA CB C 17.7 0.20 1
311 . 42 ALA HB H 1.29 0.02 1
312 . 43 GLY N N 107.5 0.25 1
313 . 43 GLY H H 8.45 0.02 1
314 . 43 GLY CA C 47.8 0.20 1
315 . 43 GLY HA2 H 4.22 0.02 2
316 . 43 GLY HA3 H 3.94 0.02 2
317 . 44 LYS N N 123.4 0.25 1
318 . 44 LYS H H 7.91 0.02 1
319 . 44 LYS CA C 58.5 0.20 1
320 . 44 LYS HA H 4.41 0.02 1
321 . 44 LYS CB C 32.5 0.20 1
322 . 44 LYS HB2 H 1.78 0.02 2
323 . 44 LYS HB3 H 1.68 0.02 2
324 . 44 LYS HG2 H 1.57 0.02 1
325 . 44 LYS HG3 H 1.57 0.02 1
326 . 45 ILE N N 121.5 0.25 1
327 . 45 ILE H H 8.98 0.02 1
328 . 45 ILE CA C 66.2 0.20 1
329 . 45 ILE HA H 3.64 0.02 1
330 . 45 ILE CB C 38.2 0.20 1
331 . 45 ILE HB H 1.69 0.02 1
332 . 45 ILE HG2 H 0.59 0.02 1
333 . 45 ILE HG12 H 1.46 0.02 2
334 . 45 ILE HD1 H 0.82 0.02 1
335 . 46 THR N N 116.2 0.25 1
336 . 46 THR H H 7.92 0.02 1
337 . 46 THR CA C 68.2 0.20 1
338 . 46 THR HA H 3.66 0.02 1
339 . 46 THR CB C 68.8 0.20 1
340 . 46 THR HB H 4.37 0.02 1
341 . 46 THR HG2 H 1.26 0.02 1
342 . 47 GLY N N 106.5 0.25 1
343 . 47 GLY H H 7.79 0.02 1
344 . 47 GLY CA C 47.6 0.20 1
345 . 47 GLY HA2 H 3.90 0.02 2
346 . 47 GLY HA3 H 3.68 0.02 2
347 . 48 MET N N 119.8 0.25 1
348 . 48 MET H H 7.83 0.02 1
349 . 48 MET CA C 59.3 0.20 1
350 . 48 MET HA H 4.15 0.02 1
351 . 48 MET CB C 33.9 0.20 1
352 . 48 MET HB2 H 2.21 0.02 2
353 . 48 MET HB3 H 2.15 0.02 2
354 . 48 MET HG2 H 2.79 0.02 2
355 . 48 MET HG3 H 2.58 0.02 2
356 . 49 ILE N N 121.6 0.25 1
357 . 49 ILE H H 7.87 0.02 1
358 . 49 ILE CA C 65.3 0.20 1
359 . 49 ILE HA H 3.69 0.02 1
360 . 49 ILE CB C 38.2 0.20 1
361 . 49 ILE HB H 1.90 0.02 1
362 . 49 ILE HG2 H 0.86 0.02 1
363 . 49 ILE HD1 H 0.72 0.02 1
364 . 50 LEU N N 117.0 0.25 1
365 . 50 LEU H H 8.07 0.02 1
366 . 50 LEU CA C 56.2 0.20 1
367 . 50 LEU HA H 4.01 0.02 1
368 . 50 LEU CB C 42.3 0.20 1
369 . 50 LEU HB2 H 1.75 0.02 2
370 . 50 LEU HB3 H 1.66 0.02 2
371 . 50 LEU HD1 H 0.86 0.02 2
372 . 50 LEU HD2 H 0.79 0.02 2
373 . 51 ASP N N 117.9 0.25 1
374 . 51 ASP H H 7.15 0.02 1
375 . 51 ASP CA C 55.3 0.20 1
376 . 51 ASP HA H 4.69 0.02 1
377 . 51 ASP CB C 41.3 0.20 1
378 . 51 ASP HB2 H 2.71 0.02 1
379 . 51 ASP HB3 H 2.71 0.02 1
380 . 52 LEU N N 122.6 0.25 1
381 . 52 LEU H H 7.61 0.02 1
382 . 52 LEU CA C 54.1 0.20 1
383 . 52 LEU HA H 4.40 0.02 1
384 . 52 LEU CB C 40.6 0.20 1
385 . 52 LEU HB2 H 1.95 0.02 2
386 . 52 LEU HB3 H 1.86 0.02 2
387 . 52 LEU HG H 1.26 0.02 1
388 . 52 LEU HD1 H 0.92 0.02 2
389 . 52 LEU HD2 H 0.84 0.02 2
390 . 54 PRO CA C 66.2 0.20 1
391 . 54 PRO HA H 4.00 0.02 1
392 . 54 PRO CB C 32.0 0.20 1
393 . 55 GLN N N 114.2 0.25 1
394 . 55 GLN H H 8.96 0.02 1
395 . 55 GLN CA C 58.6 0.20 1
396 . 55 GLN HA H 4.24 0.02 1
397 . 55 GLN CB C 27.7 0.20 1
398 . 55 GLN HB2 H 2.14 0.02 1
399 . 55 GLN HB3 H 2.14 0.02 1
400 . 55 GLN HG2 H 2.58 0.02 2
401 . 55 GLN HG3 H 2.44 0.02 2
402 . 55 GLN HE21 H 6.97 0.02 2
403 . 55 GLN HE22 H 7.72 0.02 2
404 . 56 GLU N N 118.2 0.25 1
405 . 56 GLU H H 8.10 0.02 1
406 . 56 GLU CA C 56.9 0.20 1
407 . 56 GLU HA H 4.32 0.02 1
408 . 56 GLU CB C 31.0 0.20 1
409 . 56 GLU HB2 H 2.15 0.02 2
410 . 56 GLU HB3 H 1.99 0.02 2
411 . 56 GLU HG2 H 2.32 0.02 1
412 . 56 GLU HG3 H 2.32 0.02 1
413 . 57 VAL N N 119.8 0.25 1
414 . 57 VAL H H 7.51 0.02 1
415 . 57 VAL CA C 65.1 0.20 1
416 . 57 VAL HA H 3.67 0.02 1
417 . 57 VAL CB C 32.5 0.20 1
418 . 57 VAL HB H 1.85 0.02 1
419 . 57 VAL HG1 H 0.90 0.02 2
420 . 57 VAL HG2 H 0.78 0.02 2
421 . 58 PHE N N 118.5 0.25 1
422 . 58 PHE H H 7.85 0.02 1
423 . 58 PHE CA C 59.1 0.20 1
424 . 58 PHE HA H 4.30 0.02 1
425 . 58 PHE CB C 36.9 0.20 1
426 . 58 PHE HB2 H 3.21 0.02 2
427 . 58 PHE HB3 H 3.08 0.02 2
428 . 58 PHE HD1 H 7.30 0.02 3
429 . 59 PRO CA C 66.1 0.20 1
430 . 59 PRO CB C 32.0 0.20 1
431 . 60 LEU N N 115.4 0.25 1
432 . 60 LEU H H 7.68 0.02 1
433 . 60 LEU CA C 57.4 0.20 1
434 . 60 LEU HA H 4.20 0.02 1
435 . 60 LEU CB C 41.2 0.20 1
436 . 60 LEU HB2 H 2.14 0.02 2
437 . 60 LEU HB3 H 2.09 0.02 2
438 . 60 LEU HG H 1.63 0.02 1
439 . 60 LEU HD1 H 0.74 0.02 2
440 . 60 LEU HD2 H 0.60 0.02 2
441 . 61 LEU N N 114.9 0.25 1
442 . 61 LEU H H 7.53 0.02 1
443 . 61 LEU HA H 3.98 0.02 1
444 . 61 LEU CB C 41.0 0.20 1
445 . 61 LEU HB2 H 1.90 0.02 2
446 . 61 LEU HB3 H 1.61 0.02 2
447 . 61 LEU HG H 1.77 0.02 1
448 . 61 LEU HD1 H 0.91 0.02 2
449 . 61 LEU HD2 H 0.71 0.02 2
450 . 62 GLU N N 115.5 0.25 1
451 . 62 GLU H H 7.16 0.02 1
452 . 62 GLU CA C 56.4 0.20 1
453 . 62 GLU HA H 4.45 0.02 1
454 . 62 GLU CB C 31.8 0.20 1
455 . 62 GLU HB2 H 1.89 0.02 1
456 . 62 GLU HB3 H 1.89 0.02 1
457 . 62 GLU HG2 H 2.24 0.02 2
458 . 62 GLU HG3 H 2.17 0.02 2
459 . 63 SER N N 113.6 0.25 1
460 . 63 SER H H 7.33 0.02 1
461 . 63 SER CA C 55.8 0.20 1
462 . 63 SER HA H 4.90 0.02 1
463 . 63 SER CB C 63.6 0.20 1
464 . 63 SER HB2 H 3.96 0.02 2
465 . 63 SER HB3 H 3.87 0.02 2
466 . 64 ASP N N 131.5 0.25 1
467 . 64 ASP H H 9.08 0.02 1
468 . 64 ASP CA C 58.0 0.20 1
469 . 64 ASP HA H 4.65 0.02 1
470 . 64 ASP CB C 40.6 0.20 1
471 . 64 ASP HB2 H 2.80 0.02 2
472 . 64 ASP HB3 H 2.68 0.02 2
473 . 65 GLU N N 120.5 0.25 1
474 . 65 GLU H H 8.65 0.02 1
475 . 65 GLU CA C 60.0 0.20 1
476 . 65 GLU HA H 4.14 0.02 1
477 . 65 GLU CB C 29.7 0.20 1
478 . 65 GLU HB2 H 2.05 0.02 2
479 . 65 GLU HB3 H 1.95 0.02 2
480 . 65 GLU HG2 H 2.32 0.02 1
481 . 65 GLU HG3 H 2.32 0.02 1
482 . 66 LEU N N 120.6 0.25 1
483 . 66 LEU H H 7.90 0.02 1
484 . 66 LEU CA C 57.6 0.20 1
485 . 66 LEU HA H 4.30 0.02 1
486 . 66 LEU CB C 42.4 0.20 1
487 . 66 LEU HB2 H 1.85 0.02 2
488 . 66 LEU HB3 H 1.80 0.02 2
489 . 66 LEU HG H 1.62 0.02 1
490 . 66 LEU HD1 H 1.05 0.02 2
491 . 66 LEU HD2 H 0.94 0.02 2
492 . 67 PHE N N 121.3 0.25 1
493 . 67 PHE H H 8.71 0.02 1
494 . 67 PHE CA C 63.6 0.20 1
495 . 67 PHE HA H 4.12 0.02 1
496 . 67 PHE CB C 38.2 0.20 1
497 . 67 PHE HB2 H 3.95 0.02 2
498 . 67 PHE HB3 H 3.30 0.02 2
499 . 67 PHE HD1 H 7.20 0.02 3
500 . 67 PHE HZ H 6.95 0.02 1
501 . 68 GLU N N 119.8 0.25 1
502 . 68 GLU H H 8.94 0.02 1
503 . 68 GLU CA C 60.0 0.20 1
504 . 68 GLU HA H 3.76 0.02 1
505 . 68 GLU CB C 29.2 0.20 1
506 . 68 GLU HB2 H 2.25 0.02 2
507 . 68 GLU HB3 H 2.16 0.02 2
508 . 68 GLU HG2 H 2.53 0.02 2
509 . 68 GLU HG3 H 2.44 0.02 2
510 . 69 GLN N N 118.3 0.25 1
511 . 69 GLN H H 7.70 0.02 1
512 . 69 GLN CA C 59.4 0.20 1
513 . 69 GLN HA H 4.05 0.02 1
514 . 69 GLN CB C 28.7 0.20 1
515 . 69 GLN HB2 H 2.25 0.02 2
516 . 69 GLN HB3 H 2.12 0.02 2
517 . 69 GLN HG2 H 2.44 0.02 1
518 . 69 GLN HG3 H 2.44 0.02 1
519 . 70 HIS N N 117.0 0.25 1
520 . 70 HIS H H 7.81 0.02 1
521 . 70 HIS CA C 59.9 0.20 1
522 . 70 HIS HA H 4.26 0.02 1
523 . 70 HIS CB C 29.1 0.20 1
524 . 70 HIS HB2 H 3.01 0.02 1
525 . 70 HIS HB3 H 3.01 0.02 1
526 . 70 HIS HD2 H 7.23 0.02 1
527 . 70 HIS HE1 H 8.41 0.02 1
528 . 71 TYR N N 123.1 0.25 1
529 . 71 TYR H H 9.40 0.02 1
530 . 71 TYR CA C 63.0 0.20 1
531 . 71 TYR HA H 3.63 0.02 1
532 . 71 TYR CB C 38.0 0.20 1
533 . 71 TYR HB2 H 2.66 0.02 2
534 . 71 TYR HB3 H 2.07 0.02 2
535 . 71 TYR HD1 H 6.84 0.02 3
536 . 71 TYR HE1 H 6.77 0.02 3
537 . 72 LYS N N 121.3 0.25 1
538 . 72 LYS H H 8.41 0.02 1
539 . 72 LYS CA C 60.4 0.20 1
540 . 72 LYS HA H 3.74 0.02 1
541 . 72 LYS CB C 32.5 0.20 1
542 . 72 LYS HB2 H 1.99 0.02 2
543 . 72 LYS HB3 H 1.92 0.02 2
544 . 72 LYS HG2 H 1.73 0.02 1
545 . 72 LYS HG3 H 1.73 0.02 1
546 . 72 LYS HD2 H 1.47 0.02 1
547 . 72 LYS HD3 H 1.47 0.02 1
548 . 73 GLU N N 118.7 0.25 1
549 . 73 GLU H H 7.28 0.02 1
550 . 73 GLU CA C 59.3 0.20 1
551 . 73 GLU HA H 4.05 0.02 1
552 . 73 GLU CB C 30.0 0.20 1
553 . 73 GLU HB2 H 2.03 0.02 1
554 . 73 GLU HB3 H 2.03 0.02 1
555 . 73 GLU HG2 H 2.39 0.02 2
556 . 73 GLU HG3 H 2.23 0.02 2
557 . 74 ALA N N 123.4 0.25 1
558 . 74 ALA H H 8.24 0.02 1
559 . 74 ALA CA C 54.8 0.20 1
560 . 74 ALA HA H 4.28 0.02 1
561 . 74 ALA CB C 19.7 0.20 1
562 . 74 ALA HB H 1.42 0.02 1
563 . 75 SER N N 113.8 0.25 1
564 . 75 SER H H 8.72 0.02 1
565 . 75 SER CA C 62.5 0.20 1
566 . 75 SER HA H 3.93 0.02 1
567 . 75 SER CB C 62.6 0.20 1
568 . 75 SER HB2 H 3.52 0.02 2
569 . 75 SER HB3 H 3.48 0.02 2
570 . 76 ALA N N 123.8 0.25 1
571 . 76 ALA H H 7.57 0.02 1
572 . 76 ALA CA C 55.2 0.20 1
573 . 76 ALA HA H 4.21 0.02 1
574 . 76 ALA CB C 18.1 0.20 1
575 . 76 ALA HB H 1.50 0.02 1
576 . 77 ALA N N 122.4 0.25 1
577 . 77 ALA H H 7.75 0.02 1
578 . 77 ALA CA C 55.1 0.20 1
579 . 77 ALA HA H 4.17 0.02 1
580 . 77 ALA CB C 18.2 0.20 1
581 . 77 ALA HB H 1.52 0.02 1
582 . 78 TYR N N 121.5 0.25 1
583 . 78 TYR H H 8.67 0.02 1
584 . 78 TYR CA C 61.5 0.20 1
585 . 78 TYR HA H 4.18 0.02 1
586 . 78 TYR CB C 38.6 0.20 1
587 . 78 TYR HB2 H 3.15 0.02 2
588 . 78 TYR HB3 H 3.05 0.02 2
589 . 78 TYR HD1 H 7.09 0.02 3
590 . 78 TYR HE1 H 6.78 0.02 3
591 . 79 GLU N N 119.0 0.25 1
592 . 79 GLU H H 8.38 0.02 1
593 . 79 GLU CA C 59.4 0.20 1
594 . 79 GLU HA H 3.76 0.02 1
595 . 79 GLU CB C 29.4 0.20 1
596 . 79 GLU HB2 H 2.08 0.02 1
597 . 79 GLU HB3 H 2.08 0.02 1
598 . 79 GLU HG2 H 2.45 0.02 1
599 . 79 GLU HG3 H 2.45 0.02 1
600 . 80 SER N N 115.0 0.25 1
601 . 80 SER H H 7.91 0.02 1
602 . 80 SER CA C 61.7 0.20 1
603 . 80 SER HA H 4.19 0.02 1
604 . 80 SER CB C 63.2 0.20 1
605 . 80 SER HB2 H 3.95 0.02 1
606 . 80 SER HB3 H 3.95 0.02 1
607 . 81 PHE N N 123.4 0.25 1
608 . 81 PHE H H 7.91 0.02 1
609 . 81 PHE CA C 60.0 0.20 1
610 . 81 PHE HA H 4.18 0.02 1
611 . 81 PHE CB C 38.4 0.20 1
612 . 81 PHE HB2 H 3.22 0.02 1
613 . 81 PHE HB3 H 3.22 0.02 1
614 . 81 PHE HD1 H 7.21 0.02 3
615 . 82 LYS N N 120.6 0.25 1
616 . 82 LYS H H 8.10 0.02 1
617 . 82 LYS CA C 58.3 0.20 1
618 . 82 LYS HA H 3.77 0.02 1
619 . 82 LYS CB C 31.9 0.20 1
620 . 82 LYS HB2 H 1.64 0.02 2
621 . 82 LYS HB3 H 1.55 0.02 2
622 . 82 LYS HG2 H 1.21 0.02 1
623 . 82 LYS HG3 H 1.21 0.02 1
624 . 83 LYS N N 119.8 0.25 1
625 . 83 LYS H H 7.78 0.02 1
626 . 83 LYS CA C 58.4 0.20 1
627 . 83 LYS HA H 4.09 0.02 1
628 . 83 LYS CB C 32.5 0.20 1
629 . 83 LYS HB2 H 1.87 0.02 1
630 . 83 LYS HB3 H 1.87 0.02 1
631 . 83 LYS HG2 H 1.65 0.02 2
632 . 83 LYS HG3 H 1.54 0.02 2
633 . 84 GLU N N 120.0 0.25 1
634 . 84 GLU H H 7.88 0.02 1
635 . 84 GLU CA C 58.4 0.20 1
636 . 84 GLU HA H 4.09 0.02 1
637 . 84 GLU CB C 29.8 0.20 1
638 . 84 GLU HB2 H 2.03 0.02 1
639 . 84 GLU HB3 H 2.03 0.02 1
640 . 84 GLU HG2 H 2.35 0.02 2
641 . 84 GLU HG3 H 2.23 0.02 2
642 . 85 GLN N N 118.8 0.25 1
643 . 85 GLN H H 7.90 0.02 1
644 . 85 GLN CA C 57.3 0.20 1
645 . 85 GLN HA H 4.08 0.02 1
646 . 85 GLN CB C 29.4 0.20 1
647 . 85 GLN HB2 H 2.03 0.02 2
648 . 85 GLN HB3 H 1.89 0.02 2
649 . 85 GLN HG2 H 2.13 0.02 1
650 . 85 GLN HG3 H 2.13 0.02 1
651 . 86 GLU N N 120.5 0.25 1
652 . 86 GLU H H 7.98 0.02 1
653 . 86 GLU CA C 57.6 0.20 1
654 . 86 GLU HA H 4.17 0.02 1
655 . 86 GLU CB C 30.1 0.20 1
656 . 86 GLU HB2 H 2.04 0.02 1
657 . 86 GLU HB3 H 2.04 0.02 1
658 . 86 GLU HG2 H 2.37 0.02 2
659 . 86 GLU HG3 H 2.25 0.02 2
660 . 87 GLN N N 119.8 0.25 1
661 . 87 GLN H H 8.03 0.02 1
662 . 87 GLN CA C 56.5 0.20 1
663 . 87 GLN HA H 4.28 0.02 1
664 . 87 GLN CB C 29.4 0.20 1
665 . 87 GLN HB2 H 2.14 0.02 2
666 . 87 GLN HB3 H 2.04 0.02 2
667 . 87 GLN HG2 H 2.41 0.02 1
668 . 87 GLN HG3 H 2.41 0.02 1
669 . 88 GLN N N 121.1 0.25 1
670 . 88 GLN H H 8.20 0.02 1
671 . 88 GLN CA C 56.2 0.20 1
672 . 88 GLN HA H 4.38 0.02 1
673 . 88 GLN CB C 29.4 0.20 1
674 . 88 GLN HB2 H 2.14 0.02 2
675 . 88 GLN HB3 H 2.04 0.02 2
676 . 88 GLN HG2 H 2.41 0.02 1
677 . 88 GLN HG3 H 2.41 0.02 1
678 . 89 THR N N 115.6 0.25 1
679 . 89 THR H H 8.12 0.02 1
680 . 89 THR CA C 62.3 0.20 1
681 . 89 THR HA H 4.32 0.02 1
682 . 89 THR CB C 70.0 0.20 1
683 . 89 THR HB H 4.22 0.02 1
684 . 89 THR HG2 H 1.22 0.02 1
685 . 90 GLU N N 123.6 0.25 1
686 . 90 GLU H H 8.38 0.02 1
687 . 90 GLU CA C 56.8 0.20 1
688 . 90 GLU HA H 4.32 0.02 1
689 . 90 GLU CB C 30.6 0.20 1
690 . 91 GLN N N 122.5 0.25 1
691 . 91 GLN H H 8.35 0.02 1
692 . 91 GLN CA C 55.9 0.20 1
693 . 91 GLN CB C 29.8 0.20 1
694 . 92 ALA N N 132.2 0.25 1
695 . 92 ALA H H 8.01 0.02 1
696 . 92 ALA CA C 54.0 0.20 1
697 . 92 ALA CB C 20.3 0.20 1
stop_
save_
########################
# Coupling constants #
########################
save_J_values_set_1
_Saveframe_category coupling_constants
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_1
_Spectrometer_frequency_1H 500
_Mol_system_component_name 'PABC domain'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 3 LEU H 3 LEU HA 7.1 . . 0.5
2 3JHNHA 4 GLY H 4 GLY HA 7.9 . . 0.5
3 3JHNHA 5 SER H 5 SER HA 7.4 . . 0.5
4 3JHNHA 7 ARG H 7 ARG HA 7.1 . . 0.5
5 3JHNHA 8 ASN H 8 ASN HA 8.0 . . 0.5
6 3JHNHA 9 ALA H 9 ALA HA 5.4 . . 0.5
7 3JHNHA 10 ASN H 10 ASN HA 8.1 . . 0.5
8 3JHNHA 11 ASP H 11 ASP HA 6.8 . . 0.5
9 3JHNHA 12 ASN H 12 ASN HA 7.6 . . 0.5
10 3JHNHA 14 GLN H 14 GLN HA 6.8 . . 0.5
11 3JHNHA 15 PHE H 15 PHE HA 6.4 . . 0.5
12 3JHNHA 16 TYR H 16 TYR HA 6.6 . . 0.5
13 3JHNHA 17 GLN H 17 GLN HA 5.9 . . 0.5
14 3JHNHA 18 GLN H 18 GLN HA 4.4 . . 0.5
15 3JHNHA 19 LYS H 19 LYS HA 5.2 . . 0.5
16 3JHNHA 22 GLN H 22 GLN HA 4.7 . . 0.5
17 3JHNHA 23 ALA H 23 ALA HA 4.5 . . 0.5
18 3JHNHA 25 GLY H 25 GLY HA 6.1 . . 0.5
19 3JHNHA 26 GLU H 26 GLU HA 4.9 . . 0.5
20 3JHNHA 27 GLN H 27 GLN HA 4.0 . . 0.5
21 3JHNHA 28 LEU H 28 LEU HA 5.3 . . 0.5
22 3JHNHA 29 TYR H 29 TYR HA 5.2 . . 0.5
23 3JHNHA 30 LYS H 30 LYS HA 4.2 . . 0.5
24 3JHNHA 31 LYS H 31 LYS HA 6.1 . . 0.5
25 3JHNHA 32 VAL H 32 VAL HA 4.6 . . 0.5
26 3JHNHA 33 SER H 33 SER HA 3.9 . . 0.5
27 3JHNHA 34 ALA H 34 ALA HA 5.6 . . 0.5
28 3JHNHA 35 LYS H 35 LYS HA 9.7 . . 0.5
29 3JHNHA 37 SER H 37 SER HA 8.0 . . 0.5
30 3JHNHA 38 ASN H 38 ASN HA 4.3 . . 0.5
31 3JHNHA 39 GLU H 39 GLU HA 4.1 . . 0.5
32 3JHNHA 40 GLU H 40 GLU HA 5.1 . . 0.5
33 3JHNHA 41 ALA H 41 ALA HA 4.5 . . 0.5
34 3JHNHA 43 GLY H 43 GLY HA 6.3 . . 0.5
35 3JHNHA 44 LYS H 44 LYS HA 3.7 . . 0.5
36 3JHNHA 47 GLY H 47 GLY HA 6.1 . . 0.5
37 3JHNHA 48 MET H 48 MET HA 5.2 . . 0.5
38 3JHNHA 49 ILE H 49 ILE HA 5.9 . . 0.5
39 3JHNHA 50 LEU H 50 LEU HA 5.0 . . 0.5
40 3JHNHA 51 ASP H 51 ASP HA 7.2 . . 0.5
41 3JHNHA 52 LEU H 52 LEU HA 6.6 . . 0.5
42 3JHNHA 55 GLN H 55 GLN HA 4.0 . . 0.5
43 3JHNHA 57 VAL H 57 VAL HA 7.6 . . 0.5
44 3JHNHA 60 LEU H 60 LEU HA 6.2 . . 0.5
45 3JHNHA 61 LEU H 61 LEU HA 6.3 . . 0.5
46 3JHNHA 62 GLU H 62 GLU HA 9.6 . . 0.5
47 3JHNHA 64 ASP H 64 ASP HA 3.6 . . 0.5
48 3JHNHA 65 GLU H 65 GLU HA 4.2 . . 0.5
49 3JHNHA 66 LEU H 66 LEU HA 4.7 . . 0.5
50 3JHNHA 69 GLN H 69 GLN HA 4.1 . . 0.5
51 3JHNHA 70 HIS H 70 HIS HA 6.4 . . 0.5
52 3JHNHA 73 GLU H 73 GLU HA 4.9 . . 0.5
53 3JHNHA 74 ALA H 74 ALA HA 4.9 . . 0.5
54 3JHNHA 75 SER H 75 SER HA 4.3 . . 0.5
55 3JHNHA 76 ALA H 76 ALA HA 4.2 . . 0.5
56 3JHNHA 77 ALA H 77 ALA HA 5.1 . . 0.5
57 3JHNHA 80 SER H 80 SER HA 5.7 . . 0.5
58 3JHNHA 81 PHE H 81 PHE HA 3.6 . . 0.5
59 3JHNHA 83 LYS H 83 LYS HA 5.7 . . 0.5
60 3JHNHA 84 GLU H 84 GLU HA 5.9 . . 0.5
61 3JHNHA 85 GLN H 85 GLN HA 6.4 . . 0.5
62 3JHNHA 86 GLU H 86 GLU HA 6.3 . . 0.5
63 3JHNHA 87 GLN H 87 GLN HA 7.6 . . 0.5
64 3JHNHA 88 GLN H 88 GLN HA 7.0 . . 0.5
65 3JHNHA 89 THR H 89 THR HA 8.5 . . 0.5
66 3JHNHA 90 GLU H 90 GLU HA 6.6 . . 0.5
67 3JHNHA 91 GLN H 91 GLN HA 7.1 . . 0.5
68 3JHNHA 92 ALA H 92 ALA HA 7.3 . . 0.5
stop_
save_